Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism

ABCG2 is a transporter contributing to multidrug resistance of cancer cells. Here, structures of human ABCG2 under turnover conditions reveal distinct conformational states, provide insight into the transport cycle and suggest a mechanism of discrimination between substrates and inhibitors.

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Autores principales:	Qin Yu, Dongchun Ni, Julia Kowal, Ioannis Manolaridis, Scott M. Jackson, Henning Stahlberg, Kaspar P. Locher
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f3dae0a3a07a42eb9d31262f294b2505
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spelling	oai:doaj.org-article:f3dae0a3a07a42eb9d31262f294b25052021-12-02T16:26:40ZStructures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism10.1038/s41467-021-24651-22041-1723https://doaj.org/article/f3dae0a3a07a42eb9d31262f294b25052021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24651-2https://doaj.org/toc/2041-1723ABCG2 is a transporter contributing to multidrug resistance of cancer cells. Here, structures of human ABCG2 under turnover conditions reveal distinct conformational states, provide insight into the transport cycle and suggest a mechanism of discrimination between substrates and inhibitors.Qin YuDongchun NiJulia KowalIoannis ManolaridisScott M. JacksonHenning StahlbergKaspar P. LocherNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Qin Yu Dongchun Ni Julia Kowal Ioannis Manolaridis Scott M. Jackson Henning Stahlberg Kaspar P. Locher Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
description	ABCG2 is a transporter contributing to multidrug resistance of cancer cells. Here, structures of human ABCG2 under turnover conditions reveal distinct conformational states, provide insight into the transport cycle and suggest a mechanism of discrimination between substrates and inhibitors.
format	article
author	Qin Yu Dongchun Ni Julia Kowal Ioannis Manolaridis Scott M. Jackson Henning Stahlberg Kaspar P. Locher
author_facet	Qin Yu Dongchun Ni Julia Kowal Ioannis Manolaridis Scott M. Jackson Henning Stahlberg Kaspar P. Locher
author_sort	Qin Yu
title	Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
title_short	Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
title_full	Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
title_fullStr	Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
title_full_unstemmed	Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
title_sort	structures of abcg2 under turnover conditions reveal a key step in the drug transport mechanism
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f3dae0a3a07a42eb9d31262f294b2505
work_keys_str_mv	AT qinyu structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism AT dongchunni structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism AT juliakowal structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism AT ioannismanolaridis structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism AT scottmjackson structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism AT henningstahlberg structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism AT kasparplocher structuresofabcg2underturnoverconditionsrevealakeystepinthedrugtransportmechanism
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Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism

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